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Conserved domains on  [gi|755929187|ref|XP_011309885|]
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leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 3 [Fopius arisanus]

Protein Classification

LRR and Ig domain-containing protein( domain architecture ID 11469616)

LRR and Ig domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
105-382 1.03e-28

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 120.04  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 105 LSTPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQisvlpyqGFIVVKSLIN 184
Cdd:COG4886   45 LLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLES 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 185 LDLTGNRIVSLPDHtFKPNRQLLVLQLSSNRLTKLPSRLlSGLTNLQHLDMSSNDIEILPRSFfAELSRLEYLDVSGNPI 264
Cdd:COG4886  118 LDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 265 VNLSNtAFQGLNSLLSINLGRTRLMRLPkdlwtpvpelrslildqtriellrnDDLIGLSNLENLTISNSPLRGLESktL 344
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLP-------------------------EPLANLTNLETLDLSNNQLTDLPE--L 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755929187 345 NHLSHLRNLNLRSNDLTFLPaSLAHLKRLEHLHLEGNP 382
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQ 283
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 448-546 1.25e-09

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd04969:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWvtpqleifhwnpdpSFpdafhdhpshhgvhDTTNLGNSGHVRLMENGSLLITNLLRQDVGRY 527
Cdd:cd04969   19 DVIIECKPKASPKPTISW--------------SK--------------GTELLTNSSRICILPDGSLKIKNVTKSDEGKY 70

                         90
                 ....*....|....*....
gi 755929187 528 KCFAVNPIANMTTFVYLKM 546
Cdd:cd04969   71 TCFAVNFFGKANSTGSLSV 89
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
105-382 1.03e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 120.04  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 105 LSTPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQisvlpyqGFIVVKSLIN 184
Cdd:COG4886   45 LLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLES 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 185 LDLTGNRIVSLPDHtFKPNRQLLVLQLSSNRLTKLPSRLlSGLTNLQHLDMSSNDIEILPRSFfAELSRLEYLDVSGNPI 264
Cdd:COG4886  118 LDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 265 VNLSNtAFQGLNSLLSINLGRTRLMRLPkdlwtpvpelrslildqtriellrnDDLIGLSNLENLTISNSPLRGLESktL 344
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLP-------------------------EPLANLTNLETLDLSNNQLTDLPE--L 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755929187 345 NHLSHLRNLNLRSNDLTFLPaSLAHLKRLEHLHLEGNP 382
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQ 283
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 180-382 3.87e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 180 KSLINLDLTGNRIVSLPDhtFKPNRQLLVLQLSSNRLTKLPSrlLSGLTNLQHLDMSSNDIEILPrsFFAELSRLEYLDV 259
Cdd:cd21340    2 KRITHLYLNDKNITKIDN--LSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 260 SGNPIVNLSNtaFQGLNSLLSINLGRTRLmrlpkdlwtpvPELRSLILDQTRIELLRNddliglsNLENLTISNSPLRGL 339
Cdd:cd21340   76 GGNRISVVEG--LENLTNLEELHIENQRL-----------PPGEKLTFDPRSLAALSN-------SLRVLNISGNNIDSL 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755929187 340 ESktLNHLSHLRNLNLRSNDLTFLPA---SLAHLKRLEHLHLEGNP 382
Cdd:cd21340  136 EP--LAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNP 179
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
58-312 7.06e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.89  E-value: 7.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  58 LPQSAINVVLINVRAAQLPVTAlesSDSLERLVWCSSGIERLePGVFLSTplLDHLDLGDNRIASLPEDVLAPLHRlryL 137
Cdd:PRK15370 197 IPEQITTLILDNNELKSLPENL---QGNIKTLYANSNQLTSI-PATLPDT--IQEMELSINRITELPERLPSALQS---L 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 138 NLTANSLTTLPRSALQGldsLETLLLAHNQISVLPYQgfiVVKSLINLDLTGNRIVSLPDhTFKPNrqLLVLQLSSNRLT 217
Cdd:PRK15370 268 DLFHNKISCLPENLPEE---LRYLSVYDNSIRTLPAH---LPSGITHLNVQSNSLTALPE-TLPPG--LKTLEAGENALT 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 218 KLPSRLLSGltnLQHLDMSSNDIEILPRSFFAELSRleyLDVSGNPIVNLSNTAFQGLNSLLSinlGRTRLMRLPKDLwt 297
Cdd:PRK15370 339 SLPASLPPE---LQVLDVSKNQITVLPETLPPTITT---LDVSRNALTNLPENLPAALQIMQA---SRNNLVRLPESL-- 407

                        250
                 ....*....|....*
gi 755929187 298 pvPELRSLILDQTRI 312
Cdd:PRK15370 408 --PHFRGEGPQPTRI 420
LRR_8 pfam13855
Leucine rich repeat;
181-240 2.18e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.54  E-value: 2.18e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  181 SLINLDLTGNRIVSLPDHTFKPNRQLLVLQLSSNRLTKLPSRLLSGLTNLQHLDMSSNDI 240
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 448-546 1.25e-09

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWvtpqleifhwnpdpSFpdafhdhpshhgvhDTTNLGNSGHVRLMENGSLLITNLLRQDVGRY 527
Cdd:cd04969   19 DVIIECKPKASPKPTISW--------------SK--------------GTELLTNSSRICILPDGSLKIKNVTKSDEGKY 70

                         90
                 ....*....|....*....
gi 755929187 528 KCFAVNPIANMTTFVYLKM 546
Cdd:cd04969   71 TCFAVNFFGKANSTGSLSV 89
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 436-533 4.84e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  436 ATNTETQHRLNSSVLLECEFNGNPAPSLTWVtpqleifhwnpdpsfpdaFHDHPSHHGVHDTTNLGNSghvrlmeNGSLL 515
Cdd:pfam13927   6 VSPSSVTVREGETVTLTCEATGSPPPTITWY------------------KNGEPISSGSTRSRSLSGS-------NSTLT 60

                          90
                  ....*....|....*...
gi 755929187  516 ITNLLRQDVGRYKCFAVN 533
Cdd:pfam13927  61 ISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 444-545 6.25e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 6.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187   444 RLNSSVLLECEFNGNPAPSLTWVTPQLEIfhwnpdPSFPDAFHDHPSHHgvhdttnlgnsghvrlmeNGSLLITNLLRQD 523
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKL------LAESGRFSVSRSGS------------------TSTLTISNVTPED 62

                           90       100
                   ....*....|....*....|..
gi 755929187   524 VGRYKCFAVNPIANMTTFVYLK 545
Cdd:smart00410  63 SGTYTCAATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
105-382 1.03e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 120.04  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 105 LSTPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQisvlpyqGFIVVKSLIN 184
Cdd:COG4886   45 LLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-------ELSNLTNLES 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 185 LDLTGNRIVSLPDHtFKPNRQLLVLQLSSNRLTKLPSRLlSGLTNLQHLDMSSNDIEILPRSFfAELSRLEYLDVSGNPI 264
Cdd:COG4886  118 LDLSGNQLTDLPEE-LANLTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQI 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 265 VNLSNtAFQGLNSLLSINLGRTRLMRLPkdlwtpvpelrslildqtriellrnDDLIGLSNLENLTISNSPLRGLESktL 344
Cdd:COG4886  195 TDLPE-PLGNLTNLEELDLSGNQLTDLP-------------------------EPLANLTNLETLDLSNNQLTDLPE--L 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 755929187 345 NHLSHLRNLNLRSNDLTFLPaSLAHLKRLEHLHLEGNP 382
Cdd:COG4886  247 GNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
63-378 4.25e-28

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 118.11  E-value: 4.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  63 INVVLINVRAAQLPVTALESSDSLERLVWCSSGIERLEPGVFLSTPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTAN 142
Cdd:COG4886   27 LLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 143 SlttlprsALQGLDSLETLLLAHNQISVLPyQGFIVVKSLINLDLTGNRIVSLPDhTFKPNRQLLVLQLSSNRLTKLPSr 222
Cdd:COG4886  107 E-------ELSNLTNLESLDLSGNQLTDLP-EELANLTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDLPE- 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 223 LLSGLTNLQHLDMSSNDIEILPRSFfAELSRLEYLDVSGNPIVNLSNtAFQGLNSLLSINLGRTRLMRLP--KDLwtpvP 300
Cdd:COG4886  177 ELGNLTNLKELDLSNNQITDLPEPL-GNLTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLPelGNL----T 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755929187 301 ELRSLILDQTRIELLrnDDLIGLSNLENLTISNSPLRGLESKTLNHLSHLRNLNLRSNDLTFLPASLAHLKRLEHLHL 378
Cdd:COG4886  251 NLEELDLSNNQLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
107-381 6.22e-24

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 105.40  E-value: 6.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 107 TPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQISVLPYQgfIVVKSLINLD 186
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLL--LSLLLLLLLS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 187 LTGNRIVSLPDHTFKPNRQLLVLQLSSNRLtklpsrlLSGLTNLQHLDMSSNDIEILPRSFfAELSRLEYLDVSGNPIVN 266
Cdd:COG4886   79 LLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLTD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 267 LSnTAFQGLNSLLSINLGRTRLMRLPKDLwTPVPELRSLILDQTRIELLrNDDLIGLSNLENLTISNSPLRGLeSKTLNH 346
Cdd:COG4886  151 LP-EPLGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLAN 226

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 755929187 347 LSHLRNLNLRSNDLTFLPaSLAHLKRLEHLHLEGN 381
Cdd:COG4886  227 LTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
110-374 9.72e-23

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.93  E-value: 9.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 110 LDHLDLGDNRIASLPEDvLAPLHRLRYLNLTANSLTTLPrSALQGLDSLETLLLAHNQISVLPyQGFIVVKSLINLDLTG 189
Cdd:COG4886  161 LKSLDLSNNQLTDLPEE-LGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQLTDLP-EPLANLTNLETLDLSN 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 190 NRIVSLPDhtFKPNRQLLVLQLSSNRLTKLPSrlLSGLTNLQHLDMSSNDIEILprsffaELSRLEYLDVSGNPIVNLSN 269
Cdd:COG4886  238 NQLTDLPE--LGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLTDL------KLKELELLLGLNSLLLLLLL 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 270 TAFQGLNSLLSINLGRTRLMRLPKDLWTPVPELRSLILDQTRIELLRNDDLIGLSNLENLTISNSPLRGLESKTLNHLSH 349
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLL 387

                        250       260
                 ....*....|....*....|....*
gi 755929187 350 LRNLNLRSNDLTFLPASLAHLKRLE 374
Cdd:COG4886  388 TLLLLLLTTTAGVLLLTLALLDAVN 412
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
78-341 5.53e-16

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.13  E-value: 5.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  78 TALESSDSLERLVWCSSGIERLePGVFLSTPLLDHLDLGDNRIASLPEdVLAPLHRLRYLNLTANSLTTLPRSaLQGLDS 157
Cdd:COG4886  153 EPLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLPEP-LANLTN 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 158 LETLLLAHNQISVLPYqgFIVVKSLINLDLTGNRIVSLPDHTFKPNrqLLVLQLSSNRLTKLPSRLL---SGLTNLQHLD 234
Cdd:COG4886  230 LETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPPLANLTN--LKTLDLSNNQLTDLKLKELellLGLNSLLLLL 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 235 MSSNDIEILPRSFFAELSRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRLMRLPKDLWTPVPELRSLILDQTRIEL 314
Cdd:COG4886  306 LLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALL 385

                        250       260
                 ....*....|....*....|....*..
gi 755929187 315 LRNDDLIGLSNLENLTISNSPLRGLES 341
Cdd:COG4886  386 LLTLLLLLLTTTAGVLLLTLALLDAVN 412
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 180-382 3.87e-15

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 75.21  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 180 KSLINLDLTGNRIVSLPDhtFKPNRQLLVLQLSSNRLTKLPSrlLSGLTNLQHLDMSSNDIEILPrsFFAELSRLEYLDV 259
Cdd:cd21340    2 KRITHLYLNDKNITKIDN--LSLCKNLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIE--NLENLVNLKKLYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 260 SGNPIVNLSNtaFQGLNSLLSINLGRTRLmrlpkdlwtpvPELRSLILDQTRIELLRNddliglsNLENLTISNSPLRGL 339
Cdd:cd21340   76 GGNRISVVEG--LENLTNLEELHIENQRL-----------PPGEKLTFDPRSLAALSN-------SLRVLNISGNNIDSL 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755929187 340 ESktLNHLSHLRNLNLRSNDLTFLPA---SLAHLKRLEHLHLEGNP 382
Cdd:cd21340  136 EP--LAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNP 179
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
58-312 7.06e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.89  E-value: 7.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  58 LPQSAINVVLINVRAAQLPVTAlesSDSLERLVWCSSGIERLePGVFLSTplLDHLDLGDNRIASLPEDVLAPLHRlryL 137
Cdd:PRK15370 197 IPEQITTLILDNNELKSLPENL---QGNIKTLYANSNQLTSI-PATLPDT--IQEMELSINRITELPERLPSALQS---L 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 138 NLTANSLTTLPRSALQGldsLETLLLAHNQISVLPYQgfiVVKSLINLDLTGNRIVSLPDhTFKPNrqLLVLQLSSNRLT 217
Cdd:PRK15370 268 DLFHNKISCLPENLPEE---LRYLSVYDNSIRTLPAH---LPSGITHLNVQSNSLTALPE-TLPPG--LKTLEAGENALT 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 218 KLPSRLLSGltnLQHLDMSSNDIEILPRSFFAELSRleyLDVSGNPIVNLSNTAFQGLNSLLSinlGRTRLMRLPKDLwt 297
Cdd:PRK15370 339 SLPASLPPE---LQVLDVSKNQITVLPETLPPTITT---LDVSRNALTNLPENLPAALQIMQA---SRNNLVRLPESL-- 407

                        250
                 ....*....|....*
gi 755929187 298 pvPELRSLILDQTRI 312
Cdd:PRK15370 408 --PHFRGEGPQPTRI 420
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 110-269 1.09e-12

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 68.27  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 110 LDHLDLGDNRIASLPEdvLAPLHRLRYLNLTANSLTTLPRsaLQGLDSLETLLLAHNQISVLpyQGFIVVKSLINLDLTG 189
Cdd:cd21340   26 LKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGNRISVV--EGLENLTNLEELHIEN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 190 NRI---VSLpdhTFKPN------RQLLVLQLSSNRLTKLpsRLLSGLTNLQHLDMSSNDI----EILPrsFFAELSRLEY 256
Cdd:cd21340  100 QRLppgEKL---TFDPRslaalsNSLRVLNISGNNIDSL--EPLAPLRNLEQLDASNNQIsdleELLD--LLSSWPSLRE 172

                        170
                 ....*....|...
gi 755929187 257 LDVSGNPIVNLSN 269
Cdd:cd21340  173 LDLTGNPVCKKPK 185
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 104-296 1.55e-12

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 69.69  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 104 FLSTPLLDHLDLGDNRIASLPEDVLA-----PLHRLRYLNLTANSLTTLP----RSALQGLDSLETLLLAHNQISV--LP 172
Cdd:cd00116  104 LLRSSSLQELKLNNNGLGDRGLRLLAkglkdLPPALEKLVLGRNRLEGAScealAKALRANRDLKELNLANNGIGDagIR 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 173 Y--QGFIVVKSLINLDLTGNRI----VSLPDHTFKPNRQLLVLQLSSNRLT-----KLPSRLLSGLTNLQHLDMSSNDIE 241
Cdd:cd00116  184 AlaEGLKANCNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNNLTdagaaALASALLSPNISLLTLSLSCNDIT 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755929187 242 ILP----RSFFAELSRLEYLDVSGNpivNLSNTAFQGLNSLLSINLGRTRLMRLPKDLW 296
Cdd:cd00116  264 DDGakdlAEVLAEKESLLELDLRGN---KFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 103-381 1.69e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 71.42  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 103 VFLSTPLLDHLDLGDNRIA-SLPEDVLAPLHRLRYLNLTANSLT-TLPRSALQGLdslETLLLAHNQISVLPYQGFIVVK 180
Cdd:PLN00113  88 AIFRLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNFTgSIPRGSIPNL---ETLDLSNNMLSGEIPNDIGSFS 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 181 SLINLDLTGNRIVSLPDHTFKPNRQLLVLQLSSNRLT-KLPSRL---------------LSG--------LTNLQHLDMS 236
Cdd:PLN00113 165 SLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELgqmkslkwiylgynnLSGeipyeiggLTSLNHLDLV 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 237 SNDIEILPRSFFAELSRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRLMrlpkdlwTPVPELrslildqtriellr 316
Cdd:PLN00113 245 YNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLS-------GEIPEL-------------- 303

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755929187 317 nddLIGLSNLENLTISNSPLRGLESKTLNHLSHLRNLNLRSNDLTF-LPASLAHLKRLEHLHLEGN 381
Cdd:PLN00113 304 ---VIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGeIPKNLGKHNNLTVLDLSTN 366
LRR_8 pfam13855
Leucine rich repeat;
181-240 2.18e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 62.54  E-value: 2.18e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  181 SLINLDLTGNRIVSLPDHTFKPNRQLLVLQLSSNRLTKLPSRLLSGLTNLQHLDMSSNDI 240
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
110-280 5.44e-12

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 69.73  E-value: 5.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 110 LDHLDLGDNRIASLPEDVLAPLhrlRYLNLTANSLTTLPRSALQGldsLETLLLAHNQISVLPYQgfiVVKSLINLDLTG 189
Cdd:PRK15370 285 LRYLSVYDNSIRTLPAHLPSGI---THLNVQSNSLTALPETLPPG---LKTLEAGENALTSLPAS---LPPELQVLDVSK 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 190 NRIVSLPDhTFKPNrqLLVLQLSSNRLTKLPSRLLSGltnLQHLDMSSNDIEILPRS---FFAELSRLEYLDVSGNPIvn 266
Cdd:PRK15370 356 NQITVLPE-TLPPT--ITTLDVSRNALTNLPENLPAA---LQIMQASRNNLVRLPESlphFRGEGPQPTRIIVEYNPF-- 427

                        170
                 ....*....|....
gi 755929187 267 lSNTAFQGLNSLLS 280
Cdd:PRK15370 428 -SERTIQNMQRLMS 440
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
137-371 7.53e-11

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 65.87  E-value: 7.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 137 LNLTANSLTTLPRSALQgldSLETLLLAHNQISVLPYQGFIVVKSLinlDLTGNRIVSLPDhTFKPNRQllVLQLSSNRL 216
Cdd:PRK15370 183 LRLKILGLTTIPACIPE---QITTLILDNNELKSLPENLQGNIKTL---YANSNQLTSIPA-TLPDTIQ--EMELSINRI 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 217 TKLPSRLLSGltnLQHLDMSSNDIEILPRSFFAElsrLEYLDVSGNPI-------------VNLSNTAFQGLNSLLSINL 283
Cdd:PRK15370 254 TELPERLPSA---LQSLDLFHNKISCLPENLPEE---LRYLSVYDNSIrtlpahlpsgithLNVQSNSLTALPETLPPGL 327

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 284 -----GRTRLMRLPKDLwtPvPELRSLILDQTRIELLrNDDLIglSNLENLTISNSPLRGLESktlNHLSHLRNLNLRSN 358
Cdd:PRK15370 328 ktleaGENALTSLPASL--P-PELQVLDVSKNQITVL-PETLP--PTITTLDVSRNALTNLPE---NLPAALQIMQASRN 398

                        250
                 ....*....|...
gi 755929187 359 DLTFLPASLAHLK 371
Cdd:PRK15370 399 NLVRLPESLPHFR 411
LRR_8 pfam13855
Leucine rich repeat;
108-168 2.33e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 2.33e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187  108 PLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQI 168
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
113-382 4.62e-10

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 63.64  E-value: 4.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 113 LDLGDNRIASLPedVLAPlhRLRYLNLTANSLTTLPRSAlqglDSLETLLLAHNQISVLPyqgfIVVKSLINLDLTGNRI 192
Cdd:PRK15387 227 LVIPDNNLTSLP--ALPP--ELRTLEVSGNQLTSLPVLP----PGLLELSIFSNPLTHLP----ALPSGLCKLWIFGNQL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 193 VSLPdhTFKPNRQllVLQLSSNRLTKLPSrLLSGLTNLQHLDMSSNDIEILPrsffaelSRLEYLDVSGNPIVNLSNTAF 272
Cdd:PRK15387 295 TSLP--VLPPGLQ--ELSVSDNQLASLPA-LPSELCKLWAYNNQLTSLPTLP-------SGLQELSVSDNQLASLPTLPS 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 273 QgLNSLLSINLGRTRLMRLPKDLwtpvpelRSLILDQTRIELLRnddlIGLSNLENLTISNSPLRGLESKTlnhlSHLRN 352
Cdd:PRK15387 363 E-LYKLWAYNNRLTSLPALPSGL-------KELIVSGNRLTSLP----VLPSELKELMVSGNRLTSLPMLP----SGLLS 426

                        250       260       270
                 ....*....|....*....|....*....|
gi 755929187 353 LNLRSNDLTFLPASLAHLKRLEHLHLEGNP 382
Cdd:PRK15387 427 LSVYRNQLTRLPESLIHLSSETTVNLEGNP 456
LRR_8 pfam13855
Leucine rich repeat;
204-264 4.85e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.99  E-value: 4.85e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187  204 RQLLVLQLSSNRLTKLPSRLLSGLTNLQHLDMSSNDIEILPRSFFAELSRLEYLDVSGNPI 264
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Ig5_Contactin cd04969
Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth ...
 448-546 1.25e-09

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409358 [Multi-domain]  Cd Length: 89  Bit Score: 55.93  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWvtpqleifhwnpdpSFpdafhdhpshhgvhDTTNLGNSGHVRLMENGSLLITNLLRQDVGRY 527
Cdd:cd04969   19 DVIIECKPKASPKPTISW--------------SK--------------GTELLTNSSRICILPDGSLKIKNVTKSDEGKY 70

                         90
                 ....*....|....*....
gi 755929187 528 KCFAVNPIANMTTFVYLKM 546
Cdd:cd04969   71 TCFAVNFFGKANSTGSLSV 89
LRR_8 pfam13855
Leucine rich repeat;
324-382 3.68e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.30  E-value: 3.68e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  324 SNLENLTISNSPLRGLESKTLNHLSHLRNLNLRSNDLTFL-PASLAHLKRLEHLHLEGNP 382
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNR 60
LRR_8 pfam13855
Leucine rich repeat;
133-192 4.84e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.30  E-value: 4.84e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  133 RLRYLNLTANSLTTLPRSALQGLDSLETLLLAHNQISVLPYQGFIVVKSLINLDLTGNRI 192
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 101-381 5.00e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 60.25  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 101 PGVFLSTPLLDhLDLGDNRIASLPEDVLAPLHRLRYLNLTANSLT-TLPRsALQGLDSLETLLLAHNQISVLPYQGFIVV 179
Cdd:PLN00113 278 PSIFSLQKLIS-LDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTgKIPV-ALTSLPRLQVLQLWSNKFSGEIPKNLGKH 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 180 KSLINLDLTGNRIVS-LPDhTFKPNRQLLVLQLSSNRLTKLPSRLLSGLTNLQHLDMSSNDIE-ILPRSFfAELSRLEYL 257
Cdd:PLN00113 356 NNLTVLDLSTNNLTGeIPE-GLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSgELPSEF-TKLPLVYFL 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 258 DVSGNPIVNLSNTAFQGLNSLLSINLGRTRLM-RLPKDLWTPvpELRSLILDQTRIELLRNDDLIGLSNLENLTISNSPL 336
Cdd:PLN00113 434 DISNNNLQGRINSRKWDMPSLQMLSLARNKFFgGLPDSFGSK--RLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKL 511

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755929187 337 RGLESKTLNHLSHLRNLNLRSNDLT-FLPASLAHLKRLEHLHLEGN 381
Cdd:PLN00113 512 SGEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQN 557
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 200-382 1.54e-08

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 57.37  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 200 FKPNRQLLVLQLSSNRLTKLPSRLL-SGLT---NLQHLDMSSNDIEILPR------SFFAELSRLEYLDVSGNPIVNLSN 269
Cdd:cd00116   19 LPKLLCLQVLRLEGNTLGEEAAKALaSALRpqpSLKELCLSLNETGRIPRglqsllQGLTKGCGLQELDLSDNALGPDGC 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 270 TAFQGLNS-----LLSIN---LGRTRLMRLPKDLWTPVPELRSLILDQTRIEllrNDDLIGLSN-------LENLTISNS 334
Cdd:cd00116   99 GVLESLLRssslqELKLNnngLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE---GASCEALAKalranrdLKELNLANN 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755929187 335 PLR--GLES--KTLNHLSHLRNLNLRSNDLT-----FLPASLAHLKRLEHLHLEGNP 382
Cdd:cd00116  176 GIGdaGIRAlaEGLKANCNLEVLDLNNNGLTdegasALAETLASLKSLEVLNLGDNN 232
LRR_8 pfam13855
Leucine rich repeat;
85-144 1.92e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.37  E-value: 1.92e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187   85 SLERLVWCSSGIERLEPGVFLSTPLLDHLDLGDNRIASLPEDVLAPLHRLRYLNLTANSL 144
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
108-280 4.50e-08

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 57.09  E-value: 4.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 108 PLLDHLDLGDNRIASLPEdVLAPLHRLRYLNLTANSLTTLPrSALQGLD-------SLETL------LLAH-NQISVLPy 173
Cdd:PRK15387 302 PGLQELSVSDNQLASLPA-LPSELCKLWAYNNQLTSLPTLP-SGLQELSvsdnqlaSLPTLpselykLWAYnNRLTSLP- 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 174 qgfIVVKSLINLDLTGNRIVSLPdhtFKPNrQLLVLQLSSNRLTKLPsRLLSGLTNLQhldMSSNDIEILPRSFFaELSR 253
Cdd:PRK15387 379 ---ALPSGLKELIVSGNRLTSLP---VLPS-ELKELMVSGNRLTSLP-MLPSGLLSLS---VYRNQLTRLPESLI-HLSS 446

                        170       180
                 ....*....|....*....|....*..
gi 755929187 254 LEYLDVSGNPivnLSNTAFQGLNSLLS 280
Cdd:PRK15387 447 ETTVNLEGNP---LSERTLQALREITS 470
LRR_8 pfam13855
Leucine rich repeat;
228-288 5.81e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.22  E-value: 5.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187  228 TNLQHLDMSSNDIEILPRSFFAELSRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRL 288
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 69-283 1.10e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 56.01  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  69 NVRAAQLPVTaLESSDSLERLVWCSSGIERLEPGVFLSTPLLDHLDLGDNRIA-SLPEDvLAPLHRLRYLNLTANSLTTL 147
Cdd:PLN00113 366 NNLTGEIPEG-LCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSgELPSE-FTKLPLVYFLDISNNNLQGR 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 148 PRSALQGLDSLETLLLAHNQIS-VLPyqGFIVVKSLINLDLTGNRIVSLPDHTFKPNRQLLVLQLSSNRLTKLPSRLLSG 226
Cdd:PLN00113 444 INSRKWDMPSLQMLSLARNKFFgGLP--DSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSS 521

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755929187 227 LTNLQHLDMSSNDIEILPRSFFAELSRLEYLDVSGNPIVNLSNTAFQGLNSLLSINL 283
Cdd:PLN00113 522 CKKLVSLDLSHNQLSGQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVNI 578
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 449-535 2.15e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 48.86  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 449 VLLECEFNGNPAPSLTWvtpqleifHWNPDPSFPDAFHDHPSHHGvhdttnlgnsghvrlmeNGSLLITNLLRQDVGRYK 528
Cdd:cd00096    1 VTLTCSASGNPPPTITW--------YKNGKPLPPSSRDSRRSELG-----------------NGTLTISNVTLEDSGTYT 55


                 ....*..
gi 755929187 529 CFAVNPI 535
Cdd:cd00096   56 CVASNSA 62
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 446-545 4.30e-07

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546 [Multi-domain]  Cd Length: 96  Bit Score: 48.85  E-value: 4.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 446 NSSVLLECEFNGNPAPSLTWVTPQleifhwnpdPSFPDAFHDhpshhgvhdttnLGNSGHVRLMENGSLLITNLLRQDVG 525
Cdd:cd20954   16 GQDVMLHCQADGFPTPTVTWKKAT---------GSTPGEYKD------------LLYDPNVRILPNGTLVFGHVQKENEG 74

                         90       100
                 ....*....|....*....|.
gi 755929187 526 RYKCFAVNPI-ANMTTFVYLK 545
Cdd:cd20954   75 HYLCEAKNGIgSGLSKVIFLK 95
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 436-533 4.84e-07

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 47.95  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  436 ATNTETQHRLNSSVLLECEFNGNPAPSLTWVtpqleifhwnpdpsfpdaFHDHPSHHGVHDTTNLGNSghvrlmeNGSLL 515
Cdd:pfam13927   6 VSPSSVTVREGETVTLTCEATGSPPPTITWY------------------KNGEPISSGSTRSRSLSGS-------NSTLT 60

                          90
                  ....*....|....*...
gi 755929187  516 ITNLLRQDVGRYKCFAVN 533
Cdd:pfam13927  61 ISNVTRSDAGTYTCVASN 78
LRR_8 pfam13855
Leucine rich repeat;
252-312 7.51e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 46.75  E-value: 7.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187  252 SRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRLMRLPKDLWTPVPELRSLILDQTRI 312
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 110-264 1.08e-06

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 52.10  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 110 LDHLDLGDNRI----ASLPEDVLAPLHRLRYLNLTANSLTT----LPRSALQGLDSLETLLLAHNQIS----VLPYQGFI 177
Cdd:COG5238  238 LTTLDLSNNQIgdegVIALAEALKNNTTVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGdegaIALAEGLQ 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 178 VVKSLINLDLTGNRI-----VSLPDHtFKPNRQLLVLQLSSNRLT----KLPSRLLSGLTNLQHLDMSSNDIEILPRSFF 248
Cdd:COG5238  318 GNKTLHTLNLAYNGIgaqgaIALAKA-LQENTTLHSLDLSDNQIGdegaIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                        170
                 ....*....|....*....
gi 755929187 249 AELS---RLEYLDVSGNPI 264
Cdd:COG5238  397 IDALqtnRLHTLILDGNLI 415
LRR_8 pfam13855
Leucine rich repeat;
300-360 1.43e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 1.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187  300 PELRSLILDQTRIELLRNDDLIGLSNLENLTISNSPLRGLESKTLNHLSHLRNLNLRSNDL 360
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
233-382 1.44e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 233 LDMSSNDIEILPRSFFAELSRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRLMRLPKDLWTPVPELRSLILDQTRI 312
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 313 ELLRNDDLIGLSNLENLTIsnspLRGLESKTLNHLSHLRNLNLRSNDLTFLPASLAHLKRLEHLHLEGNP 382
Cdd:COG4886   82 LSLLLLGLTDLGDLTNLTE----LDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQ 147
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 444-545 6.25e-06

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 45.19  E-value: 6.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187   444 RLNSSVLLECEFNGNPAPSLTWVTPQLEIfhwnpdPSFPDAFHDHPSHHgvhdttnlgnsghvrlmeNGSLLITNLLRQD 523
Cdd:smart00410   7 KEGESVTLSCEASGSPPPEVTWYKQGGKL------LAESGRFSVSRSGS------------------TSTLTISNVTPED 62

                           90       100
                   ....*....|....*....|..
gi 755929187   524 VGRYKCFAVNPIANMTTFVYLK 545
Cdd:smart00410  63 SGTYTCAATNSSGSASSGTTLT 84
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
 444-544 1.11e-05

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 44.41  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 444 RLNSSVLLECEFNGNPAPSLTWvtpqleifhwnpdpsfpdafhdhpSHHGVhdtTNLGNSGHVRLMENGSLLITNLLRQD 523
Cdd:cd20952   12 AVGGTVVLNCQATGEPVPTISW------------------------LKDGV---PLLGKDERITTLENGSLQIKGAEKSD 64

                         90       100
                 ....*....|....*....|.
gi 755929187 524 VGRYKCFAVNPIANMTTFVYL 544
Cdd:cd20952   65 TGEYTCVALNLSGEATWSAVL 85
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 252-381 1.66e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.69  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 252 SRLEYLDVSGNPIVNLSNTAFQGLNSLLSINLGRTRLM-RLPKDLWTPVPELRSLILDqtriellrNDDLIG------LS 324
Cdd:PLN00113  69 SRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSgPIPDDIFTTSSSLRYLNLS--------NNNFTGsiprgsIP 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755929187 325 NLENLTISNSPLRGLESKTLNHLSHLRNLNLRSNDLT-FLPASLAHLKRLEHLHLEGN 381
Cdd:PLN00113 141 NLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASN 198
Ig_DSCAM cd05734
Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members ...
 448-533 1.96e-05

Immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM); The members here are composed of the immunoglobulin (Ig)-like domain of Down Syndrome Cell Adhesion molecule (DSCAM). DSCAM is a cell adhesion molecule expressed largely in the developing nervous system. The gene encoding DSCAM is located at human chromosome 21q22, the locus associated with the intellectual disability phenotype of Down Syndrome. DSCAM is predicted to be the largest member of the IG superfamily. It has been demonstrated that DSCAM can mediate cation-independent homophilic intercellular adhesion.


Pssm-ID: 409397 [Multi-domain]  Cd Length: 97  Bit Score: 44.02  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWvtpqleifhwnpdpsfpdafhDHPSHHGVHDTTNLGNS-GHVRLMENGSLLITNLLRQDVGR 526
Cdd:cd05734   18 AVVLNCSADGYPPPTIVW---------------------KHSKGSGVPQFQHIVPLnGRIQLLSNGSLLIKHVLEEDSGY 76


                 ....*..
gi 755929187 527 YKCFAVN 533
Cdd:cd05734   77 YLCKVSN 83
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
 449-546 5.10e-05

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 42.46  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 449 VLLECEFNGNPAPSLTWVTPQLEIFHwnpdpsfpdafhdhpshhgvhdttnlgNSGHVRLMENGSLLITNLLRQDVGRYK 528
Cdd:cd05764   18 ATLRCKARGDPEPAIHWISPEGKLIS---------------------------NSSRTLVYDNGTLDILITTVKDTGAFT 70

                         90
                 ....*....|....*...
gi 755929187 529 CFAVNPIANMTTFVYLKM 546
Cdd:cd05764   71 CIASNPAGEATARVELHI 88
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 444-545 5.26e-05

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 43.15  E-value: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 444 RLNSSVLLECEFNGNPAPSLTWVTPQLEIfhwnpdpsfpdafhdhPSHHGVHDTTNLGN-----SGHVRLME------NG 512
Cdd:cd16091   10 LLSEDCILPCSFTPGSEVVIHWYKQDSDI----------------KVHSYYYGKDQLESqdqryRNRTSLFKdqisngNA 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755929187 513 SLLITNLLRQDVGRYKCFAVNPIANMTTFVYLK 545
Cdd:cd16091   74 SLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLK 106
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 448-546 5.83e-05

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 42.76  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWVTPqleifhwnpdpsfpdafhdhpshhGVHDTTNLGNSGHvRLMENGSLLITNLLRQDVGRY 527
Cdd:cd20969   19 TVQFVCRADGDPPPAILWLSP------------------------RKHLVSAKSNGRL-TVFPDGTLEVRYAQVQDNGTY 73

                         90
                 ....*....|....*....
gi 755929187 528 KCFAVNPIANMTTFVYLKM 546
Cdd:cd20969   74 LCIAANAGGNDSMPAHLHV 92
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
 447-540 7.46e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 42.18  E-value: 7.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 447 SSVLLECEFNGNPAPSLTWVTpqleifhwnpdpsfpdafhdhpshhgvhDTTNLGNSGHVRLMENG---SLLITNLLRQD 523
Cdd:cd20972   17 SKVRLECRVTGNPTPVVRWFC----------------------------EGKELQNSPDIQIHQEGdlhSLIIAEAFEED 68

                         90
                 ....*....|....*..
gi 755929187 524 VGRYKCFAVNPIANMTT 540
Cdd:cd20972   69 TGRYSCLATNSVGSDTT 85
LRR_9 pfam14580
Leucine-rich repeat;
233-356 1.21e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 43.60  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  233 LDMSSNDIEILpRSFFAELSRLEYLDVSGNPIVNLSNtaFQGLNSLLSINLGRTRLMRLPKDLWTPVPELRSLILDQTRI 312
Cdd:pfam14580  24 LDLRGYKIPII-ENLGATLDQFDTIDFSDNEIRKLDG--FPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755929187  313 -ELLRNDDLIGLSNLENLTISNSPLRGLE---SKTLNHLSHLRNLNLR 356
Cdd:pfam14580 101 qELGDLDPLASLKKLTFLSLLRNPVTNKPhyrLYVIYKVPQLRLLDFR 148
I-set pfam07679
Immunoglobulin I-set domain;
447-534 1.97e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 41.09  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  447 SSVLLECEFNGNPAPSLTWVTPQLEIfhwnpdpsfpdafhdHPSHHgvHDTTNLGNsghvrlmeNGSLLITNLLRQDVGR 526
Cdd:pfam07679  16 ESARFTCTVTGTPDPEVSWFKDGQPL---------------RSSDR--FKVTYEGG--------TYTLTISNVQPDDSGK 70


                  ....*...
gi 755929187  527 YKCFAVNP 534
Cdd:pfam07679  71 YTCVATNS 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 441-545 2.21e-04

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 40.84  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 441 TQHRLNSSVLLECEFNGNPAPSLTWvtpqleifhwnpdpsfpdafhdhpSHHGVHDTTNLGNSghvrLMENGSLLITNLL 520
Cdd:cd20978   11 VVVKGGQDVTLPCQVTGVPQPKITW------------------------LHNGKPLQGPMERA----TVEDGTLTIINVQ 62

                         90       100
                 ....*....|....*....|....*
gi 755929187 521 RQDVGRYKCFAVNPIANMTTFVYLK 545
Cdd:cd20978   63 PEDTGYYGCVATNEIGDIYTETLLH 87
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
 448-533 2.25e-04

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 40.94  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 448 SVLLECEFNGNPAPSLTWvtpqleifhwnpdpsfpdAFHDHPshhgVHDttnlgNSGHVRLMENG---SLLITNLLRQDV 524
Cdd:cd05744   17 LCRFDCKVSGLPTPDLFW------------------QLNGKP----VRP-----DSAHKMLVRENgrhSLIIEPVTKRDA 69


                 ....*....
gi 755929187 525 GRYKCFAVN 533
Cdd:cd05744   70 GIYTCIARN 78
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 144-381 2.84e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 44.40  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 144 LTTLPRSALQGLDslETLLLAHNQISVLpyQGFIVVKSLIN-----LDLTGNRI-----VSLPDHTFKPNrQLLVLQLSS 213
Cdd:COG5238  143 LIQVLKDPLGGNA--VHLLGLAARLGLL--AAISMAKALQNnsvetVYLGCNQIgdegiEELAEALTQNT-TVTTLWLKR 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 214 NRLTKLPS----RLLSGLTNLQHLDMSSNDIEILPRSFFAEL----SRLEYLDVSGNPI----VNLSNTAFQGLNSLLSI 281
Cdd:COG5238  218 NPIGDEGAeilaEALKGNKSLTTLDLSNNQIGDEGVIALAEAlknnTTVETLYLSGNQIgaegAIALAKALQGNTTLTSL 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 282 NLGRTRL-----MRLPKDLWTPVPeLRSLILDQTRIellRNDDLIGL-------SNLENLTISNSPL--RGLES--KTLN 345
Cdd:COG5238  298 DLSVNRIgdegaIALAEGLQGNKT-LHTLNLAYNGI---GAQGAIALakalqenTTLHSLDLSDNQIgdEGAIAlaKYLE 373

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 755929187 346 HLSHLRNLNLRSNDLTFLPAS--LAHLK--RLEHLHLEGN 381
Cdd:COG5238  374 GNTTLRELNLGKNNIGKQGAEalIDALQtnRLHTLILDGN 413
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 180-379 3.66e-04

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 44.48  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  180 KSLINLDLTGNRIVSLPD--HTFKPNRQLlVLQLSSNrLTKLPSrlLSGLTNLQHLDMS--SNDIEiLPRSFfAELSRLE 255
Cdd:PLN03210  611 ENLVKLQMQGSKLEKLWDgvHSLTGLRNI-DLRGSKN-LKEIPD--LSMATNLETLKLSdcSSLVE-LPSSI-QYLNKLE 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187  256 YLDVSGnpIVNLSNTAfQGLN--SLLSINL-GRTRLMRLPkDLWTPVPELrslILDQTRIELLRNDdlIGLSNLENLTIS 332
Cdd:PLN03210  685 DLDMSR--CENLEILP-TGINlkSLYRLNLsGCSRLKSFP-DISTNISWL---DLDETAIEEFPSN--LRLENLDELILC 755

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755929187  333 NSPLRGLESKT------LNHLSH-LRNLNLRSN-DLTFLPASLAHLKRLEHLHLE 379
Cdd:PLN03210  756 EMKSEKLWERVqpltplMTMLSPsLTRLFLSDIpSLVELPSSIQNLHKLEHLEIE 810
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 466-534 9.05e-04

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 39.05  E-value: 9.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755929187 466 VTPQLEIFHWNPDPSFPDAFHDHPSHH--GVHDTTNLGNSGHVRLMENGSLLITNLLRQDVGRYKCFAVNP 534
Cdd:cd20957    6 IDPPVQTVDFGRTAVFNCSVTGNPIHTvlWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQCFVRND 76
IgI_4_Neogenin_like cd05723
Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set ...
 433-537 1.18e-03

Fourth immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues, and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409388  Cd Length: 84  Bit Score: 38.72  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 433 LTHATNTETQHRLNssVLLECEFNGNPAPSLTWVTpqleifhwNPDPSFPdafhdhpshhgvhdttnlgnSGHVRLMENG 512
Cdd:cd05723    1 LKKPSNIYAHESMD--IVFECEVTGKPTPTVKWVK--------NGDVVIP--------------------SDYFKIVKEH 50

                         90       100
                 ....*....|....*....|....*
gi 755929187 513 SLLITNLLRQDVGRYKCFAVNPIAN 537
Cdd:cd05723   51 NLQVLGLVKSDEGFYQCIAENDVGN 75
Ig5_Contactin-1 cd05852
Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth ...
 449-533 2.73e-03

Fifth immunoglobulin (Ig) domain of contactin-1; The members here are composed of the fifth immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma.


Pssm-ID: 409438  Cd Length: 89  Bit Score: 37.67  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755929187 449 VLLECEFNGNPAPSLTWVTpqleifhwnpdpsfpdafhdhpshhgvhDTTNLGNSGHVRLMENGSLLITNLLRQDVGRYK 528
Cdd:cd05852   20 VIIECKPKAAPKPKFSWSK----------------------------GTELLVNNSRISIWDDGSLEILNITKLDEGSYT 71


                 ....*
gi 755929187 529 CFAVN 533
Cdd:cd05852   72 CFAEN 76
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 205-244 3.27e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 3.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 755929187  205 QLLVLQLSSNRLTKLPsrLLSGLTNLQHLDMSSN----DIEILP 244
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNnkitDLSDLA 43
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 505-533 4.77e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 37.00  E-value: 4.77e-03
                         10        20
                 ....*....|....*....|....*....
gi 755929187 505 HVRLMENGSLLITNLLRQDVGRYKCFAVN 533
Cdd:cd05724   45 RVRIVDDGNLLIAEARKSDEGTYKCVATN 73
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 228-265 9.02e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 34.91  E-value: 9.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755929187  228 TNLQHLDMSSNDIEILPrsFFAELSRLEYLDVSGNPIV 265
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNKI 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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